3GP3
Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine
Summary for 3GP3
| Entry DOI | 10.2210/pdb3gp3/pdb |
| Related | 3EZN 3FDZ 3GP5 3GW8 |
| Descriptor | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, TETRAETHYLENE GLYCOL, PHOSPHITE ION, ... (5 entities in total) |
| Functional Keywords | phosphoglyceromutase, decode, sbri, niaid, uwppg, glycolysis, isomerase, structural genomics, seattle structural genomics center for infectious disease, ssgcid |
| Biological source | Burkholderia pseudomallei (Pseudomonas pseudomallei) |
| Total number of polymer chains | 4 |
| Total formula weight | 118056.91 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-03-20, release date: 2009-03-31, Last modification date: 2024-02-21) |
| Primary citation | Davies, D.R.,Staker, B.L.,Abendroth, J.A.,Edwards, T.E.,Hartley, R.,Leonard, J.,Kim, H.,Rychel, A.L.,Hewitt, S.N.,Myler, P.J.,Stewart, L.J. An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Acta Crystallogr.,Sect.F, 67:1044-1050, 2011 Cited by PubMed Abstract: Burkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported. PubMed: 21904048DOI: 10.1107/S1744309111030405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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